{"id":10321,"date":"2026-07-03T17:39:42","date_gmt":"2026-07-03T17:39:42","guid":{"rendered":"https:\/\/kapdec.com\/help\/?p=10321"},"modified":"2026-07-03T17:39:42","modified_gmt":"2026-07-03T17:39:42","slug":"environmental-impacts-on-enzyme-function","status":"publish","type":"post","link":"https:\/\/kapdec.com\/help\/environmental-impacts-on-enzyme-function\/","title":{"rendered":"Environmental Impacts On Enzyme Function"},"content":{"rendered":"<div class=\"article-watermark-wrapper\">\n<div style=\"position: relative; z-index: 1;\">\n<p style=\"font-family: Arial, Helvetica, Calibri, sans-serif; font-size: 9pt; color: #444444;\">KAPDEC&reg; | Elite STEM Learning Platform | <a href=\"https:\/\/kapdec.com\" target=\"_blank\" rel=\"noopener noreferrer\" style=\"color: #444444; text-decoration: underline;\">https:\/\/kapdec.com<\/a><\/p>\n<hr \/>\n<h2><strong>Unit: Cellular energetics<\/strong><\/h2>\n<h3><strong>Chapter: Environmental impacts on enzyme function<\/strong><\/h3>\n<p><strong><em>Reference:<\/em><\/strong> <em>Temperature, Hydrogen -ion concentration, Concentration of the enzymes, Concentration of the substrate, Concentration of the end products, Hydration<strong> <\/strong><\/em><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Learning objectives<\/strong><\/p>\n<ul>\n<li>To understand the effect of environment on enzymes<\/li>\n<\/ul>\n<p>The presence of enzymes not only accelerates or retards the chemical reactions but due to their high specificity they are able to regulate several chemical reactions taking place in a cell simultaneously. In other words, enzyme specificity causes an independent control of each reaction.<\/p>\n<p>Each enzymatic reaction, like all reactions is again governed by a few factors and the influence of all these factors upon enzymatic reactions.<\/p>\n<p><strong>Temperature-<\/strong>it is one of the most important factors which control effectively the rate of enzymatic reactions.<\/p>\n<ul>\n<li>At 0 degree C, the rate of an enzyme-catalysed reaction is practically zero<\/li>\n<li>The enzymatic reactions rise with the rise in temperature up to 40 degrees<\/li>\n<li>The increased temperature has got either a direct effect on the reaction system or it may have some effect on the structure of the enzyme.<\/li>\n<li>The optimum temperature for an enzymatic reaction lies between 30-40 degrees<\/li>\n<li>Activity or the rate of reaction decreases at higher temperature which favours the partial inactivation of the enzymes. The enzymes are destroyed due to protein denaturation<\/li>\n<\/ul>\n<p><strong>Hydrogen -ion concentration<\/strong>&#8211; the enzymes are very restricted in their activity by the hydrogen-ion concentration of the medium in which they are acting<\/p>\n<ul>\n<li>The optimum Ph value for the enzymatic activity varies considerably<\/li>\n<li>The pH 7.5 is found to be optimum for the conversion of malic acid to fumaric acid, but for the reverse reaction the optimum pH is about 6.2<\/li>\n<li>The general range of pH values for the enzymatic activity varies from pH 1.5-10.0<\/li>\n<li>At higher or lower pH values the enzymes are inactivated, first reversibly and then irreversibly, causing an ultimate decrease in the activity.<\/li>\n<li>Changes in the pH cause denaturation of the enzyme molecule resulting in the decrease of enzymatic activity<\/li>\n<\/ul>\n<p><strong>Concentration of the enzymes<\/strong><\/p>\n<ul>\n<li>If there is an excess substrate available and the pH, temperature and other conditions are not limiting, then there is a linear relationship between the concentration of the enzymes and the rate of enzymatic reactions i.e., by doubling the number of enzymes the activity can also be increased.<\/li>\n<li>Increasing the enzyme concentration, in fact, increase the number of available active sites, thus increasing the chance of reactive contact between enzyme and substrate<\/li>\n<\/ul>\n<p><strong>Concentration of the substrate<\/strong><\/p>\n<ul>\n<li>Increase in the substrate concentration causes an increase in the number of reacting molecules in the vicinity of the enzyme&rsquo;s active sites which therefore increase the rate of an enzyme catalysed reaction<\/li>\n<li>The increase in substrate molecules in the reaction, causes an active accumulation of end products, which until and unless are removed cannot accelerate the reaction rate<\/li>\n<\/ul>\n<p><strong>Concentration of the end products<\/strong><\/p>\n<ul>\n<li>Like all chemical reactions, the enzymatic reactions also follow the laws of chemical equilibrium, which means that the active accumulation of the end products will cause a decrease in the reaction rate.<\/li>\n<li>The velocity of the enzymatic reactions, therefore, depends on the speed with which the products are removed from the medium.<\/li>\n<\/ul>\n<p><strong>Hydration <\/strong><\/p>\n<ul>\n<li>The amount of water in the medium may have a direct effect on the enzymatic activity<\/li>\n<li>During germination, the activity of the enzymes increases due to increase in the hydration of the tissues<\/li>\n<\/ul>\n<p><strong>Solved examples<\/strong><\/p>\n<p><strong>Example 1<\/strong>. At high temperatures, the rate of enzyme action decreases because the increased heat&#8230;&#8230;<\/p>\n<p>a) neutralizes the acids and bases in the system<\/p>\n<p>b) alters the shape of the active site of the enzyme<\/p>\n<p>c) increases the concentration of the enzyme<\/p>\n<p>d) changes the pH of the system<\/p>\n<p><strong>Solution 1: &nbsp;<\/strong>b. At high temperatures, the rate of enzyme action decreases because the increased heat alters the shape of the active site of the enzyme<\/p>\n<p><strong>Example 2<\/strong>. How does an increase in substrate affect reaction rate?<\/p>\n<p>a) Decrease forever b) Increase forever<\/p>\n<p>c) Decrease until enzyme saturated d) Increase until enzyme saturated<\/p>\n<p><strong>Solution 2: <\/strong>Increase in substrate increases the reaction rate until enzyme is saturated.<\/p>\n<p><strong>&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp; Summary<\/strong><\/p>\n<ul>\n<li>Enzyme specificity causes an independent control of each reaction<\/li>\n<li>The optimum temperature for an enzymatic reaction lies between 30-40 degrees<\/li>\n<li>The general range of pH values for the enzymatic activity varies from pH 1.5-10.0<\/li>\n<li>Increasing the enzyme concentration, in fact, increases the number of available active sites<\/li>\n<li>Increase in the substrate concentration causes an increase in the number of reacting molecules in the vicinity of the enzyme&rsquo;s active sites which therefore increase the rate of an enzyme catalysed reaction<\/li>\n<li>The active accumulation of the end products will cause a decrease in the reaction rate.<\/li>\n<li>The amount of water in the medium may have a direct effect on the enzymatic activity<\/li>\n<\/ul>\n<p>&nbsp;<\/p>\n<p><!--kapdec-footer-start--><\/p>\n<style>.kapdec-article-footer{font-family:Arial,Helvetica,Calibri,sans-serif;color:#444;}.kapdec-footer-grid{display:flex;align-items:stretch;border:1px solid #e5e7eb;border-radius:6px;overflow:hidden;}.kapdec-footer-left,.kapdec-qr-block{flex:1 1 50%;width:50%;box-sizing:border-box;min-width:0;}.kapdec-footer-left{padding:22px 28px;border-right:1px solid #e5e7eb;}.kapdec-citation-block{line-height:1.6;font-size:9pt;color:#333;margin:0;}.kapdec-citation-block p{margin:0 0 10px 0;}.kapdec-citation-block a{color:#0066cc;text-decoration:underline;}.kapdec-copyright-block{margin-top:18px;padding-top:14px;border-top:1px solid #e5e7eb;font-size:7.5pt;color:#777;line-height:1.55;text-align:left;}.kapdec-copyright-block p{margin:0 0 5px 0;}.kapdec-qr-block{padding:22px 28px;display:flex;flex-direction:column;align-items:center;justify-content:center;text-align:center;}.kapdec-qr-label{margin:0 0 8px 0;font-size:8.5pt;font-weight:600;color:#444;line-height:1.35;letter-spacing:.02em;}.kapdec-qr-url{margin:0 0 14px 0;font-size:7.5pt;line-height:1.4;color:#777;word-break:break-word;max-width:100%;}.kapdec-qr-url a{color:#777;text-decoration:underline;}@media (max-width:640px){.kapdec-footer-grid{flex-direction:column;}.kapdec-footer-left,.kapdec-qr-block{width:100%;flex-basis:100%;border-right:none;}.kapdec-footer-left{border-bottom:1px solid #e5e7eb;}}<\/style>\n<div class=\"kapdec-article-footer\" style=\"margin-top: 28px; padding-top: 4px;\">\n<div class=\"kapdec-footer-grid\">\n<div class=\"kapdec-footer-left\">\n<div class=\"kapdec-citation-block\">\n<p>A Kapdec&reg; learning guide &#8211; Crafted by elite STEM mentors for ambitious learners.<\/p>\n<p><a href=\"https:\/\/kapdec.com\" target=\"_blank\" rel=\"noopener noreferrer\">Learn more at https:\/\/kapdec.com<\/a><\/p>\n<\/div>\n<div class=\"kapdec-copyright-block\">\n<p>Author: Kapdec | Publisher: Kapdec | Copyright: &copy; Kapdec. 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